ADCY10

Protein-coding gene in the species Homo sapiens

More reference expression dataBioGPS


More reference expression data

Gene ontology
Molecular function	nucleotide binding manganese ion binding metal ion binding lyase activity adenylate cyclase activity phosphorus-oxygen lyase activity bicarbonate binding ATP binding magnesium ion binding ATPase binding
Cellular component	cytoplasm cytosol cell projection membrane microtubule cytoskeleton growth cone basal part of cell plasma membrane apical part of cell cilium axon neuronal cell body dendrite mitochondrion perinuclear region of cytoplasm motile cilium cytoskeleton nucleus apical plasma membrane extracellular region
Biological process	cellular response to inorganic substance intracellular signal transduction epithelial cilium movement involved in extracellular fluid movement cyclic nucleotide biosynthetic process spermatogenesis positive regulation of apoptotic process cAMP biosynthetic process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


55811


271639

Ensembl


ENSG00000143199


ENSMUSG00000026567

UniProt


Q96PN6


Q8C0T9

RefSeq (mRNA)


NM_001167749 NM_001297772 NM_018417


NM_173029 NM_001357427

RefSeq (protein)


NP_001161221 NP_001284701 NP_060887


NP_766617 NP_001344356

Location (UCSC)

Chr 1: 167.81 – 167.91 Mb

Chr 1: 165.31 – 165.4 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Adenylyl cyclase 10 also known as ADCY10 is an enzyme that, in humans, is encoded by the ADCY10 gene.^[5]

Function

The protein encoded by this gene belongs to a distinct class of mammalian adenylyl cyclase that is soluble and insensitive to G protein or forskolin regulation. It is localized in the cytoplasm and is thought to function as a general bicarbonate sensor throughout the body. It may also play an important role in the generation of cAMP in spermatozoa, implying possible roles in sperm maturation through the epididymis, capacitation, hypermotility, and/or the acrosome reaction.^[6]

Clinical significance

Mutations in the ADCY10 gene are associated with an increased risk of adsorptive hypercalciuria^[5] and male infertility.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000143199 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026567 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b Reed BY, Heller HJ, Gitomer WL, Pak CY (November 1999). "Mapping a gene defect in absorptive hypercalciuria to chromosome 1q23.3-q24". The Journal of Clinical Endocrinology and Metabolism. 84 (11): 3907–3913. doi:10.1210/jcem.84.11.6155. PMID 10566627.
^ "Entrez Gene: ADCY10".
^ Akbari A, Pipitone GB, Anvar Z, Jaafarinia M, Ferrari M, Carrera P, et al. (June 2019). "ADCY10 frameshift variant leading to severe recessive asthenozoospermia and segregating with absorptive hypercalciuria". Human Reproduction. 34 (6): 1155–1164. doi:10.1093/humrep/dez048. PMID 31119281.

External links

Human ADCY10 genome location and ADCY10 gene details page in the UCSC Genome Browser.

Hukovic N, Panetta R, Kumar U, Rocheville M, Patel YC (August 1998). "The cytoplasmic tail of the human somatostatin receptor type 5 is crucial for interaction with adenylyl cyclase and in mediating desensitization and internalization". The Journal of Biological Chemistry. 273 (33): 21416–21422. doi:10.1074/jbc.273.33.21416. PMID 9694905.
Buck J, Sinclair ML, Schapal L, Cann MJ, Levin LR (January 1999). "Cytosolic adenylyl cyclase defines a unique signaling molecule in mammals". Proceedings of the National Academy of Sciences of the United States of America. 96 (1): 79–84. Bibcode:1999PNAS...96...79B. doi:10.1073/pnas.96.1.79. PMC 15096. PMID 9874775.
Hayes JS, Lawler OA, Walsh MT, Kinsella BT (August 1999). "The prostacyclin receptor is isoprenylated. Isoprenylation is required for efficient receptor-effector coupling". The Journal of Biological Chemistry. 274 (34): 23707–23718. doi:10.1074/jbc.274.34.23707. PMID 10446129.
Sinclair ML, Wang XY, Mattia M, Conti M, Buck J, Wolgemuth DJ, et al. (May 2000). "Specific expression of soluble adenylyl cyclase in male germ cells". Molecular Reproduction and Development. 56 (1): 6–11. doi:10.1002/(SICI)1098-2795(200005)56:1<6::AID-MRD2>3.0.CO;2-M. PMID 10737962. S2CID 34539645.
Chen Y, Cann MJ, Litvin TN, Iourgenko V, Sinclair ML, Levin LR, et al. (July 2000). "Soluble adenylyl cyclase as an evolutionarily conserved bicarbonate sensor". Science. 289 (5479): 625–628. Bibcode:2000Sci...289..625C. doi:10.1126/science.289.5479.625. PMID 10915626.
Jaiswal BS, Conti M (August 2001). "Identification and functional analysis of splice variants of the germ cell soluble adenylyl cyclase". The Journal of Biological Chemistry. 276 (34): 31698–31708. doi:10.1074/jbc.M011698200. PMID 11423534.
Reed BY, Gitomer WL, Heller HJ, Hsu MC, Lemke M, Padalino P, et al. (April 2002). "Identification and characterization of a gene with base substitutions associated with the absorptive hypercalciuria phenotype and low spinal bone density". The Journal of Clinical Endocrinology and Metabolism. 87 (4): 1476–1485. doi:10.1210/jc.87.4.1476. PMID 11932268.
Zippin JH, Chen Y, Nahirney P, Kamenetsky M, Wuttke MS, Fischman DA, et al. (January 2003). "Compartmentalization of bicarbonate-sensitive adenylyl cyclase in distinct signaling microdomains". FASEB Journal. 17 (1): 82–84. doi:10.1096/fj.02-0598fje. PMID 12475901. S2CID 22099561.
Litvin TN, Kamenetsky M, Zarifyan A, Buck J, Levin LR (May 2003). "Kinetic properties of "soluble" adenylyl cyclase. Synergism between calcium and bicarbonate". The Journal of Biological Chemistry. 278 (18): 15922–15926. doi:10.1074/jbc.M212475200. PMID 12609998.
Jaiswal BS, Conti M (September 2003). "Calcium regulation of the soluble adenylyl cyclase expressed in mammalian spermatozoa". Proceedings of the National Academy of Sciences of the United States of America. 100 (19): 10676–10681. Bibcode:2003PNAS..10010676J. doi:10.1073/pnas.1831008100. PMC 196863. PMID 12958208.
Marjanovic JA, Li Z, Stojanovic A, Du X (November 2005). "Stimulatory roles of nitric-oxide synthase 3 and guanylyl cyclase in platelet activation". The Journal of Biological Chemistry. 280 (45): 37430–37438. doi:10.1074/jbc.M506518200. PMID 16144836.
Schmid A, Sutto Z, Nlend MC, Horvath G, Schmid N, Buck J, et al. (July 2007). "Soluble adenylyl cyclase is localized to cilia and contributes to ciliary beat frequency regulation via production of cAMP". The Journal of General Physiology. 130 (1): 99–109. doi:10.1085/jgp.200709784. PMC 2154360. PMID 17591988.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Phosphorus–oxygen lyases (EC 4.6)

4.6.1

Adenylate cyclase
(4.6.1.1)

intracellular	ADCY1 ADCY2 ADCY3 ADCY4 ADCY5 ADCY6 ADCY7 ADCY8 ADCY9 ADCY10
extracellular	Extracellular adenylate cyclase

Guanylate cyclase
(4.6.1.2)

soluble guanylyl cyclase	GUCY1A2 GUCY1A3 GUCY1B2 GUCY1B3
guanylate cyclase-coupled receptor	GUCY2C GUCY2D ANP (NPR1 NPR2)

Other

Cytidylate cyclase
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
Phosphatidylinositol diacylglycerol-lyase
Glycosylphosphatidylinositol diacylglycerol-lyase
FAD-AMP lyase (cyclizing)

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)